Allosteric mechanism of haemoglobin: Rupture of salt-bridges raises the oxygen affinity of the T-structure

Journal of Molecular Biology

Volumn 281, Issue 4, 1998, Pages 581-585

  Bettati, Stefano ^a   Mozzarelli, Andrea ^a   Perutz, Max F ^b  

^a UNIVERSITY OF PARMA   (Italy)

^b MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

Allostery; Haemoglobin; Oxygen equilibria; Salt bridges

Indexed keywords

HEME; HEMOGLOBIN; HISTIDINE; LEUCINE; OXYGEN; PROTEIN SUBUNIT;

ALLOSTERISM; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; SPECTROPHOTOMETRY;

EID: 0032575762     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1983     Document Type: Article

References (21)

1. Bettati S., Mozzarelli A. T-state hemoglobin binds oxygen non-cooperatively with allosteric effects of protons, inositol hexaphosphate, and chloride. J. Biol. Chem. 272:1997;32050-32055
2. Bettati S., Kwiatkowski L.D., Kavanaugh J.S., Mozzarelli A., Arnone A., Rossi G.L., Nobel R.W. Structure and oxygen affinity of crystalline des His 146 β human hemoglobin in the T-state. J. Biol. Chem. 272:1997;33077-33084
3. Gelin B.K., Karplus M. Mechanism of tertiary structural change in hemoglobin. Proc. Natl Acad. Sci. USA. 74:1977;801-805
4. Imai K. Allosteric Effects in Haemoglobin. 1982;Cambridge University Press, Cambridge, UK
5. Kavanaugh J.S., Chafin P.R., Arnone A., Mozzarelli A., Rivetti C., Rossi G.L., Kwiatkowski L.D., Noble R. Structure and oxygen affinity of crystalline des Arg 141α human hemoglobin A in the T state. J. Mol. Biol. 248:1995;136-150
6. Liddington R., Derewenda Z., Dodson E., Hubbard R., Dodson G. High resolution crystal structures and comparisons of T-state deoxyhaemoglobins and two liganded T-state haemoglobins T(α-oxy) haemoglobin and T-(met) haemoglobin. J. Mol. Biol. 228:1992;551-579
7. Luisi B., Shibayama N. Structure of haemoglobin in the deoxy quaternary state with ligand bound at the α-haems. J. Mol. Biol. 206:1989;723-736
8. Luisi B., Liddington R., Fermi G., Shibayama N. Structure of deoxy-quaternary haemoglobin with liganded β-subunits. J. Mol. Biol. 214:1990;7-14
9. Monod J., Wyman J., Changeux J.P. On the nature of allosteric transitions a plausible model. J. Mol. Biol. 12:1965;88-118
10. Mozzarelli A., Rossi G.L. Protein function in the crystal. Annu. Rev. Biophys. Biomol. Struct. 25:1996;343-365
11. Mozzarelli A., Rivetti C., Rossi G.L., Henry E.R., Eaton W.A. Crystals of haemoglobin with the T quaternary structure bind oxygen non-cooperatively with no Bohr effect. Nature. 351:1991;416-419
12. Mozzarelli A., Rivetti C., Rossi G.L., Eaton W.A., Henry E.R. Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals. Protein Sci. 6:1997;484-489
13. Paoli M., Liddington R., Tame G., Wilkinson A., Dodson G. Crystal structure of T-state haemoglobin with oxygen bound at all four haems. J. Mol. Biol. 256:1996;775-792
14. Perutz M.F. Stereochemistry of cooperative effects in hemoglobin. Nature. 228:1970;726-739
15. Perutz M.F., Fermi G., Shih T.-b. Structure of deoxyhemoglobin Cowtown [His HC3 (146)β→Leu] origin of the alkaline Bohr effect and electrostatic interaction in hemoglobin. Proc. Natl Acad. Sci. USA. 81:1984;4781-4784
16. a values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of α-helices. J. Mol. Biol. 183:1985;491-498
17. Perutz M.F., Fermi G., Luisi B., Shaanan B., Liddington R.C. Stereochemistry of cooperative effects in hemoglobin. Accts Chem. Res. 20:1987;309-321
18. Perutz M.F., Fermi G., Poyart C., Pagnier J., Kister J. A novel allosteric mechanism in haemoglobin structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin. J. Mol. Biol. 233:1993;536-545
19. Rivetti C., Mozzarelli A., Rossi G.L., Henry E.R., Eaton W.A. Oxygen binding by single crystals of hemoglobin. Biochemistry. 32:1993;2888-2906
20. Shibayama N., Saigo S. Fixation of the quaternary structures of human adult haemoglobin by encapsulation in transparent porous silica gels. J. Mol. Biol. 251:1995;203-209
21. Shih T.-b., Jones R.T., Bonaventura J., Bonaventura C., Schneider R.G. Involvement of HisHC3(146)β in the Bohr effect of human hemoglobin. J. Biol. Chem. 259:1984;967-974